› 2llx

Solution NMR

Solution structure of the N-terminal domain of human polypeptide chain release factor eRF1

Released:
DOI: 10.2210/pdb2llx/pdb
PDB entry 2llx coloured by chain, ensemble of 20 models, front view.
PDB entry 2llx coloured by chain, ensemble of 20 models, side view.
PDB entry 2llx coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1.
Polshakov VI, Eliseev BD, Birdsall B, Frolova LY
Protein Sci 21 896-903 (2012)
PMID: 22517631

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158631 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Eukaryotic peptide chain release factor subunit 1 Chain: A
Molecule details ›
Chain: A
Length: 150 amino acids
Theoretical weight: 16.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P62495 (Residues: 1-142; Coverage: 33%)
Gene names: ERF1, ETF1, RF1, SUP45L1
Sequence domains: eRF1 domain 1
Structure domains: eRF1 domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 86%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Optimal translational termination requires C4 lysyl hydroxylation of eRF1.
Feng et al. (2014)
1 more

3 mentions without citation

Deciphering the Nonsense Readthrough Mechanism of Action of Ataluren: An in Silico Compared Study.
Tutone et al. (2019)
2 more